Amyloid fibril structure from the vascular variant of systemic AA amyloidosis

Sambhasan Banerjee; Julian Baur; Christoph Daniel; Peter Benedikt Pfeiffer; Manuel Hitzenberger; Lukas Kuhn; Sebastian Wiese; Johan Bijzet; Christian Haupt; Kerstin U. Amann; Martin Zacharias; Bouke P.C. Hazenberg; Gunilla T. Westermark; Matthias Schmidt; Marcus Fändrich

doi:10.1038/s41467-022-34636-4

Amyloid fibril structure from the vascular variant of systemic AA amyloidosis

Sambhasan Banerjee
, Julian Baur
, Christoph Daniel
, Peter Benedikt Pfeiffer
, Manuel Hitzenberger
, Lukas Kuhn
, Sebastian Wiese
, Johan Bijzet
, Christian Haupt
, Kerstin U. Amann
, Martin Zacharias
, Bouke P.C. Hazenberg
, Gunilla T. Westermark
, Matthias Schmidt
, Marcus Fändrich

Chair of Theoretical Biophysics - Biomolecular Dynamics

University of Ulm
Friedrich Alexander Universität Erlangen-Nürnberg
Technical University of Munich
University Medical Center Groningen
Uppsala University

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

Systemic AA amyloidosis is a debilitating protein misfolding disease in humans and animals. In humans, it occurs in two variants that are called ‘vascular’ and ‘glomerular’, depending on the main amyloid deposition site in the kidneys. Using cryo electron microscopy, we here show the amyloid fibril structure underlying the vascular disease variant. Fibrils purified from the tissue of such patients are mainly left-hand twisted and contain two non-equal stacks of fibril proteins. They contrast in these properties to the fibrils from the glomerular disease variant which are right-hand twisted and consist of two structurally equal stacks of fibril proteins. Our data demonstrate that the different disease variants in systemic AA amyloidosis are associated with different fibril morphologies.

Original language	English
Article number	7261
Journal	Nature Communications
Volume	13
Issue number	1
DOIs	https://doi.org/10.1038/s41467-022-34636-4
State	Published - Dec 2022

Access to Document

10.1038/s41467-022-34636-4

Cite this

Banerjee, S., Baur, J., Daniel, C., Pfeiffer, P. B., Hitzenberger, M., Kuhn, L., Wiese, S., Bijzet, J., Haupt, C., Amann, K. U., Zacharias, M., Hazenberg, B. P. C., Westermark, G. T., Schmidt, M., & Fändrich, M. (2022). Amyloid fibril structure from the vascular variant of systemic AA amyloidosis. Nature Communications, 13(1), Article 7261. https://doi.org/10.1038/s41467-022-34636-4

@article{3fdfb26573a4477e895e88d043ea47ad,

title = "Amyloid fibril structure from the vascular variant of systemic AA amyloidosis",

abstract = "Systemic AA amyloidosis is a debilitating protein misfolding disease in humans and animals. In humans, it occurs in two variants that are called {\textquoteleft}vascular{\textquoteright} and {\textquoteleft}glomerular{\textquoteright}, depending on the main amyloid deposition site in the kidneys. Using cryo electron microscopy, we here show the amyloid fibril structure underlying the vascular disease variant. Fibrils purified from the tissue of such patients are mainly left-hand twisted and contain two non-equal stacks of fibril proteins. They contrast in these properties to the fibrils from the glomerular disease variant which are right-hand twisted and consist of two structurally equal stacks of fibril proteins. Our data demonstrate that the different disease variants in systemic AA amyloidosis are associated with different fibril morphologies.",

author = "Sambhasan Banerjee and Julian Baur and Christoph Daniel and Pfeiffer, \{Peter Benedikt\} and Manuel Hitzenberger and Lukas Kuhn and Sebastian Wiese and Johan Bijzet and Christian Haupt and Amann, \{Kerstin U.\} and Martin Zacharias and Hazenberg, \{Bouke P.C.\} and Westermark, \{Gunilla T.\} and Matthias Schmidt and Marcus F{\"a}ndrich",

note = "Publisher Copyright: {\textcopyright} 2022, The Author(s).",

year = "2022",

month = dec,

doi = "10.1038/s41467-022-34636-4",

language = "English",

volume = "13",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "Nature Research",

number = "1",

}

TY - JOUR

T1 - Amyloid fibril structure from the vascular variant of systemic AA amyloidosis

AU - Banerjee, Sambhasan

AU - Baur, Julian

AU - Daniel, Christoph

AU - Pfeiffer, Peter Benedikt

AU - Hitzenberger, Manuel

AU - Kuhn, Lukas

AU - Wiese, Sebastian

AU - Bijzet, Johan

AU - Haupt, Christian

AU - Amann, Kerstin U.

AU - Zacharias, Martin

AU - Hazenberg, Bouke P.C.

AU - Westermark, Gunilla T.

AU - Schmidt, Matthias

AU - Fändrich, Marcus

PY - 2022/12

Y1 - 2022/12

N2 - Systemic AA amyloidosis is a debilitating protein misfolding disease in humans and animals. In humans, it occurs in two variants that are called ‘vascular’ and ‘glomerular’, depending on the main amyloid deposition site in the kidneys. Using cryo electron microscopy, we here show the amyloid fibril structure underlying the vascular disease variant. Fibrils purified from the tissue of such patients are mainly left-hand twisted and contain two non-equal stacks of fibril proteins. They contrast in these properties to the fibrils from the glomerular disease variant which are right-hand twisted and consist of two structurally equal stacks of fibril proteins. Our data demonstrate that the different disease variants in systemic AA amyloidosis are associated with different fibril morphologies.

AB - Systemic AA amyloidosis is a debilitating protein misfolding disease in humans and animals. In humans, it occurs in two variants that are called ‘vascular’ and ‘glomerular’, depending on the main amyloid deposition site in the kidneys. Using cryo electron microscopy, we here show the amyloid fibril structure underlying the vascular disease variant. Fibrils purified from the tissue of such patients are mainly left-hand twisted and contain two non-equal stacks of fibril proteins. They contrast in these properties to the fibrils from the glomerular disease variant which are right-hand twisted and consist of two structurally equal stacks of fibril proteins. Our data demonstrate that the different disease variants in systemic AA amyloidosis are associated with different fibril morphologies.

UR - https://www.scopus.com/pages/publications/85142505132

U2 - 10.1038/s41467-022-34636-4

DO - 10.1038/s41467-022-34636-4

M3 - Article

C2 - 36433936

AN - SCOPUS:85142505132

SN - 2041-1723

VL - 13

JO - Nature Communications

JF - Nature Communications

IS - 1

M1 - 7261

ER -

Amyloid fibril structure from the vascular variant of systemic AA amyloidosis

Abstract

Access to Document

Other files and links

Fingerprint

Cite this